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Legionella effector RavZ evades host autophagy by extracting LC3-PE from the membrane before deconjugation.

Infected cells superinduce expression of mRNA in order to initiate an immune response to a bacterial pathogen that blocks host protein synthesis.

The pseudokinase-like Legionella effector SidJ catalyzes the glutamylation of bacterial ubiquitin ligases in a calmodulin-dependent manner.

A novel bacterial deubiquitinase with multiple chain types specificity regulates the association of ubiquitinated proteins on the phagosome of Legionella pneumophila.

A novel class of bacterial OTU deubiquitinases provides insights on the distinct roles of bacterial deubiquitinases in host–pathogen interactions.

Repression of type I interferons by SP140 is essential for resistance to Legionella pneumophila and Mycobacterium tuberculosis.

Communities of bacteria that cause Legionnaire’s disease repel other bacteria by secreting an acid called HGA.

Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.

Structural and biochemical studies reveal the molecular mechanisms for ubiquitin transfer by two unique bacterial ubiquitin E3 ligases.

Caspase-11 catalytic activity and autoprocessing play key roles upstream rather than downstream of its assembly into higher-order inflammasome complexes in response to cytosolic bacterial lipopolysaccharide.